Search results for "Muscle Cells"

showing 4 items of 24 documents

Bortezomib Partially Improves Laminin α2 Chain–Deficient Muscular Dystrophy

2014

Congenital muscular dystrophy, caused by mutations in LAMA2 (the gene encoding laminin α2 chain), is a severe and incapacitating disease for which no therapy is yet available. We have recently demonstrated that proteasome activity is increased in laminin α2 chain-deficient muscle and that treatment with the nonpharmaceutical proteasome inhibitor MG-132 reduces muscle pathology in laminin α2 chain-deficient dy(3K)/dy(3K) mice. Here, we explore the use of the selective and therapeutic proteasome inhibitor bortezomib (currently used for treatment of relapsed multiple myeloma and mantle cell lymphoma) in dy(3K)/dy(3K) mice and in congenital muscular dystrophy type 1A muscle cells. Outcome measu…

Proteasome Endopeptidase ComplexApoptosisBiologyPathology and Forensic MedicineBortezomibmedicineAnimalsMyocyteMuscular dystrophyCells CulturedMultiple myelomaMuscle CellsMyogenesisBortezomibMusclesBody WeightMuscular Dystrophy Animalmedicine.diseaseBoronic AcidsFibrosisSurvival AnalysisMice Inbred C57BLDisease Models AnimalMicroRNAsGene Expression RegulationOrgan SpecificityPyrazinesCongenital muscular dystrophyCancer researchProteasome inhibitorMantle cell lymphomaLamininLocomotionmedicine.drugThe American Journal of Pathology
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Extracellular Vesicles: Delivery Vehicles of Myokines

2019

Movement and regular physical activity are two important factors that help the human body prevent, reduce and treat different chronic diseases such as obesity, type 2 diabetes, heart diseases, hypertension, sarcopenia, cachexia and cancer. During exercise, several tissues release molecules into the blood stream, and are able to mediate beneficial effects throughout the whole body. In particular, contracting skeletal muscle cells have the capacity to communicate with other organs through the release of humoral factors that play an important role in the mechanisms of adaptation to physical exercise. These muscle-derived factors, today recognized as myokines, act as endocrine and paracrine hor…

Settore BIO/17 - Istologia0301 basic medicineextracellular bodiesPhysiologyPhysical exerciseReviewexosomesExercise Muscle cells Exocytosis Extracellular bodies ExosomesExocytosislcsh:Physiology03 medical and health sciencesParacrine signalling0302 clinical medicinePhysiology (medical)MyokinemedicineMyocyteexerciselcsh:QP1-981Settore BIO/16 - Anatomia Umanabusiness.industrySkeletal musclemuscle cellsmedicine.diseaseMicrovesiclesCell biology030104 developmental biologymedicine.anatomical_structureSarcopeniabusinessexocytosis030217 neurology & neurosurgeryFrontiers in Physiology
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CO-releasing binuclear rhodium complexes as inhibitors of nitric oxide generation in stimulated macrophages.

2013

Nontoxic CO-releasing dirhodium complexes act as inhibitors of NO in stimulated macrophage cells, suggesting that novel antiinflammatory treatments could involve the use of these types of binuclear complexes.

StereochemistryAnti-Inflammatory Agentschemistry.chemical_elementApoptosisNitric OxideModels BiologicalNitric oxideRhodiumCell LineInorganic Chemistrychemistry.chemical_compoundQUIMICA ORGANICACoordination ComplexesQUIMICA ANALITICAMacrophageMoleculeAnimalsHumansRhodiumPhysical and Theoretical ChemistryCarbon monoxideCarbon MonoxideMacrophagesRegulatorQUIMICA INORGANICAMoleculesHeme oxygenaseHeme oxygenaseCormschemistrySmooth muscle cellsCell cultureApoptosisBiological AssayCarbon monoxideInorganic chemistry
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Alix protein is substrate of Ozz-E3 ligase and modulates actin remodeling in skeletal muscle

2012

Alix/AIP1 is a multifunctional adaptor protein that participates in basic cellular processes, including membrane trafficking and actin cytoskeleton assembly, by binding selectively to a variety of partner proteins. However, the mechanisms regulating Alix turnover, subcellular distribution, and function in muscle cells are unknown. We now report that Alix is expressed in skeletal muscle throughout myogenic differentiation. In myotubes, a specific pool of Alix colocalizes with Ozz, the substrate-binding component of the muscle-specific ubiquitin ligase complex Ozz-E3. We found that interaction of the two endogenous proteins in the differentiated muscle fibers changes Alix conformation and pro…

Ubiquitin-Protein LigasesMuscle Fibers Skeletalmacromolecular substancesBiochemistryCell LineMiceCell MovementTwo-Hybrid System TechniquesmedicineCell AdhesionAnimalsProtein Interaction Domains and MotifsPseudopodiaMuscle SkeletalMolecular BiologyActinMice KnockoutbiologyMyogenesisSettore BIO/16 - Anatomia UmanaCalcium-Binding ProteinsUbiquitinationActin remodelingSkeletal muscleUbiquitin-Protein Ligase ComplexesCell BiologyActin cytoskeletonUbiquitin ligaseCell biologyRepressor ProteinsActin CytoskeletonProtein Transportmedicine.anatomical_structureUbiquitin ligase complexbiology.proteinCell Migration Myogenesis Skeletal Muscle Ubiquitin Ligase Ubiquitination Alix F-actin Ozz-E3 Ubiquitin Ligase Skeletal Muscle CellsCortactinCortactinProtein Binding
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